tmRNA to the rescue Structural motives for the salvage of stalled ribosomes
(2010) In RNA Biology 7(5). p.577-581- Abstract
- During translation, mRNA molecules are incidentally damaged, leaving the ribosome unable to reach or recognize the stop codon and thus stalled with mRNA and a potentially harmful polypeptide product attached to tRNA in the ribosomal P-site. In bacteria, a process called trans-translation has evolved, where a protein-RNA complex (smpB-tmRNA) mimicks the role of aminoacyl charged tRNA in the ribosomal A-site. The ribosome then resumes protein synthesis guided by an mRNA-like portion of the tmRNA which ends with a stop codon and codes for a peptide sequence susceptible to proteolysis, thus allowing the bacteria to salvage stalled ribosomes and degrade ill-defined and potentially harmful protein products. In this article, we will recollect how... (More)
- During translation, mRNA molecules are incidentally damaged, leaving the ribosome unable to reach or recognize the stop codon and thus stalled with mRNA and a potentially harmful polypeptide product attached to tRNA in the ribosomal P-site. In bacteria, a process called trans-translation has evolved, where a protein-RNA complex (smpB-tmRNA) mimicks the role of aminoacyl charged tRNA in the ribosomal A-site. The ribosome then resumes protein synthesis guided by an mRNA-like portion of the tmRNA which ends with a stop codon and codes for a peptide sequence susceptible to proteolysis, thus allowing the bacteria to salvage stalled ribosomes and degrade ill-defined and potentially harmful protein products. In this article, we will recollect how structural studies have yielded a model for how the pre-translocation stages of trans-translation employing structural mimicry. We will also discuss possible models for (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1918195
- author
- Lindahl, Martin LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- trans-translation, tmRNA, SmpB, cryo electron microscopy, single, particle, heterogeneity analysis
- in
- RNA Biology
- volume
- 7
- issue
- 5
- pages
- 577 - 581
- publisher
- Taylor & Francis
- external identifiers
-
- wos:000288456500013
- scopus:78649368975
- ISSN
- 1547-6286
- DOI
- 10.4161/rna.7.5.13214
- language
- English
- LU publication?
- yes
- id
- 552cd1ce-1d0f-48bd-b3b5-48669a59982b (old id 1918195)
- date added to LUP
- 2016-04-01 09:48:28
- date last changed
- 2022-01-25 08:53:19
@misc{552cd1ce-1d0f-48bd-b3b5-48669a59982b,
abstract = {{During translation, mRNA molecules are incidentally damaged, leaving the ribosome unable to reach or recognize the stop codon and thus stalled with mRNA and a potentially harmful polypeptide product attached to tRNA in the ribosomal P-site. In bacteria, a process called trans-translation has evolved, where a protein-RNA complex (smpB-tmRNA) mimicks the role of aminoacyl charged tRNA in the ribosomal A-site. The ribosome then resumes protein synthesis guided by an mRNA-like portion of the tmRNA which ends with a stop codon and codes for a peptide sequence susceptible to proteolysis, thus allowing the bacteria to salvage stalled ribosomes and degrade ill-defined and potentially harmful protein products. In this article, we will recollect how structural studies have yielded a model for how the pre-translocation stages of trans-translation employing structural mimicry. We will also discuss possible models for}},
author = {{Lindahl, Martin}},
issn = {{1547-6286}},
keywords = {{trans-translation; tmRNA; SmpB; cryo electron microscopy; single; particle; heterogeneity analysis}},
language = {{eng}},
number = {{5}},
pages = {{577--581}},
publisher = {{Taylor & Francis}},
series = {{RNA Biology}},
title = {{tmRNA to the rescue Structural motives for the salvage of stalled ribosomes}},
url = {{http://dx.doi.org/10.4161/rna.7.5.13214}},
doi = {{10.4161/rna.7.5.13214}},
volume = {{7}},
year = {{2010}},
}